The diversity of immunoglobulin (Ig) functions may be explained by the peculiar structure of these flexible molecules. Heavy and light Ig chains are composed from compact stable immunoglobulin folds (IgF), or domains belonging to a large protein super family. Proteins composed from IgF have been found in various representatives of animal kingdom even those appeared during the very early stages ...

Immunoglobulin (Ig) G, IgM, IgA and IgG subclass (IgG1, IgG2, IgG3, IgG4) concentrations were determined in more than 500 healthy Turkish children using nephelometric technique. These parameters were thought to be highly varied for different ethnic groups because of environmental and genetic factors. Methodology used in previous studies has been reported to affect age-related normal values. Ser...

Antibodies are bifunctional molecules, containing a variable Fab domain that mediates binding specificity and a constant Fc domain that bridges antibody-coated targets with FcγR-expressing cells that mediate effector functions. Although traditional mechanisms of antibody-mediated neutralization of microbes have been largely thought to result from Fab-antigen interactions, recent studies suggest...

Levels of serum immunoglobulins and immunoglobulin G subclasses were measured in 32 cystic fibrosis (CF) patients, 30 asthmatics and 27 controls. When compared with the asthmatic patients and controls, the CF patients had raised levels of all IgG subclasses as well as total IgG, IgM and IgA, but there was not a statistically significant increase in IgE. The levels of immunoglobulins in the CF p...

Radioimmunoassay methods were evaluated for immunoglobulin G and immunoglobulin M antibodies against Bacteroides fragilis antigen. Of 12 serum samples from patients with B fragilis infections, 9 had higher concentrations of immunoglobulin G antibodies than any from 11 control subjects. Of 9 serum samples from infected patients, 6 had higher concentrations of immunoglobulin M than any from contr...